Evidence map›Paper›PMID 27587394›Full record

ArticleThe Journal of biological chemistry2016

ATP hydrolysis Promotes Duplex DNA Release by the RecA Presynaptic Complex.

Ja Yil Lee, Zhi Qi, Eric C Greene

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Chromosome topology gates productive RecA homology search.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. NProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. SMC protein RecN drives RecA filament translocation for in vivo homology search.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. How strand exchange protein function benefits from ATP hydrolysis.Current opinion in genetics & development · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Ja Yil LeeFrom the Department of Biochemistry & Molecular Biophysics, Columbia University, New York, New York 10032 and.
Zhi Qithe Center of Quantitative Biology & Center of Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, 100871 China.
Eric C GreeneFrom the Department of Biochemistry & Molecular Biophysics, Columbia University, New York, New York 10032 and ecg2108@cumc.columbia.edu.
Columbia University · USCenter for Life Sciences · CN

Funding

Protein purification instrumentation in support of single molecule studies of genome integrityR35GM118026 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GREENE, ERIC C · 2016 to 2025
$5.7M
NIGMS NIH HHS R35 GM118026
6 · The paper itself

Abstract

Homologous recombination is an important DNA repair pathway that plays key roles in maintaining genome stability. Escherichia coli RecA is an ATP-dependent DNA-binding protein that catalyzes the DNA strand exchange reactions in homologous recombination. RecA assembles into long helical filaments on single-stranded DNA, and these presynaptic complexes are responsible for locating and pairing with a homologous duplex DNA. Recent single molecule studies have provided new insights into RecA behavior, but the potential influence of ATP in the reactions remains poorly understood. Here we examine how ATP influences the ability of the RecA presynaptic complex to interact with homologous dsDNA. We demonstrate that over short time regimes, RecA presynaptic complexes sample heterologous dsDNA similarly in the presence of either ATP or ATPγS, suggesting that initial interactions do not depend on ATP hydrolysis. In addition, RecA stabilizes pairing intermediates in three-base steps, and stepping energetics is seemingly unaltered in the presence of ATP. However, the overall dissociation rate of these paired intermediates with ATP is ∼4-fold higher than with ATPγS. These experiments suggest that ATP plays an unanticipated role in promoting the turnover of captured duplex DNA intermediates as RecA attempts to align homologous sequences during the early stages of recombination.

Indexed as

Recombination, GeneticAdenosine TriphosphateDNA, BacterialDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsRec A RecombinasesAdenosine TriphosphateDNA, BacterialDNA, Single-StrandedEscherichia coli ProteinsRec A RecombinasesATPDNA recombinationDNA repairhomologous recombinationsingle-molecule biophysics

Identifiers

PMID27587394
PMCPMC5064001
OpenAlexW2510438185

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.